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Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

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Title: Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins
Authors: Rahman, Morshedur Browse this author
Kim, Woan-Sub Browse this author
Kumura, Haruto Browse this author →KAKEN DB
Shimazaki, Kei-ichi Browse this author
Keywords: Bifidobacteria surface proteins
Binding region
Bovine lactoferrin C-lobe
Nicked bovine lactoferrin
Issue Date: Jun-2009
Publisher: Springer Netherlands
Journal Title: Biotechnology Letters
Volume: 31
Issue: 6
Start Page: 863
End Page: 868
Publisher DOI: 10.1007/s10529-009-9936-1
PMID: 19205893
Abstract: Bovine lactoferrin (bLf) is a multifunctional iron-binding glycoprotein secreted mainly in milk and other secretory fluids. Bovine lactoferrin is reported to promote the growth of bifidobacteria and binding of bLf to bifidobacteria cell is thought to be involved. After separation of bLf half molecule and extraction of surface proteins from bifidobacteria, binding profiles were observed by immunoblotting. No binding was appeared when bLf C-lobe was being reacted with cell surface proteins on PVDF membrane. Conversely, a 50-kDa band was appeared when reacted with either intact bLf or nicked bLf. This result strongly suggests that binding region could be N-lobe. Moreover, blot, probed with nicked bLf, reacted with anti-lactoferricin antibody also produced a 50-kDa band that indicates the binding occurred at lactoferricin region of bLf molecule. Interestingly, despite absence of binding, bLf C-lobe can stimulate the growth of bifidobacteria.
Rights: The original publication is available at
Type: article (author version)
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 島崎 敬一

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